Anti myc conjugated agarose beads

Manufactured by Merck Group

Sourced in United States

Anti-Myc conjugated agarose beads are a laboratory reagent used to purify and isolate proteins that contain the Myc tag. The beads are composed of agarose, a polysaccharide derived from seaweed, and are conjugated with antibodies that specifically bind to the Myc tag. This allows for the efficient separation and capture of Myc-tagged proteins from complex mixtures, such as cell lysates or protein extracts.

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Lab products found in correlation

Anti gfp antibody, by Takara Bio (1 mentions) Anti gst antibody, by Abcam (1 mentions) Hiseq 2000, by Illumina (1 mentions) Nebnext chip seq library prep master mix set, by New England Biolabs (1 mentions) Igg sepharose 6 fast flow beads, by GE Healthcare (1 mentions) Anti flag antibody, by Merck Group (1 mentions) H3k4me3 antibody, by Merck Group (1 mentions) H3k36me3 antibody, by Abcam (1 mentions)

Spelling variants of this product

Agarose (759 citations) Anti-Myc (274 citations) Agarose beads (61 citations) Anti-Myc agarose (15 citations) Anti-Myc beads (15 citations) MYC-agarose beads (2 citations)

5 protocols using anti myc conjugated agarose beads

Co-immunoprecipitation of COP1 and SIZ1

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For co-immunoprecipitation of COP1 and SIZ1, Myc-COP1 and SIZ1-GFP were separately expressed in Col-0 protoplasts to avoid degradation of SIZ1 by COP1. Immunoprecipitation was carried out using a mixture of COP1 and SIZ1 protein extracts. The mixture of protein extracts was immunoprecipitated with anti-Myc-conjugated agarose beads (Sigma, F-2426) and co-immunoprecipitated SIZ1-GFP proteins were detected with anti-GFP antibody (Clontech, 632375).
To analyze the sumoylation effect in the interaction between HY5 and COP1, 1 μg of GST-HY5 protein purified from E. coli [52 (link)], as bait, was incubated with the protein extracts isolated from N. benthamiana co-expressing Myc-COP1 with FLAG-SUMO1 or FLAG-SUMO1^AA. The mixture of protein extracts was immunoprecipitated with anti-Myc-conjugated agarose beads (Sigma, F-2426) and co-immunoprecipitated GST-HY5 proteins were detected with anti-GST antibody (Abcam, ab19256).

Lin X.L., Niu D., Hu Z.L., Kim D.H., Jin Y.H., Cai B., Liu P., Miura K., Yun D.J., Kim W.Y., Lin R, & Jin J.B. (2016). An Arabidopsis SUMO E3 Ligase, SIZ1, Negatively Regulates Photomorphogenesis by Promoting COP1 Activity. PLoS Genetics, 12(4), e1006016.

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Chromatin Immunoprecipitation of RNAPII

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All 150-ml cell cultures were treated with formaldehyde to be a final concentration 1% for 15 min, then quenched with glycine to a final concentration of 125 mM for 5 min. The DNA-protein complexes were sheared by ultra-sound sonication, then incubated overnight with 100 μl of anti-Myc conjugated agarose beads (Sigma Aldrich, St. Louis, MO, USA, cat.# E6654), 8 μg of RNAPII Ser 5-P specific antibody (Abcam, Cambridge, MA, USA, cat.# ab5131), and 8 μg of RNAPII Ser 2-P specific antibody (Abcam, Cambridge, MA, USA, cat.# ab5095) to pull down Chd1, RNAPII Ser 5-P and, Ser 2-P, respectively. Then, for the RNAPII ChIP, 100 μl of pre-washed protein A beads were added and incubated for 4 hours. After serial wash steps, immunoprecipitated DNA was recovered with overnight incubation at 65°C water bath followed by ethanol precipitation. Subsequently, sequencing libraries were prepared using NEBNext ChIP-Seq Library Prep Master Mix Set (New England Biolabs, Ipswich, MA, USA, cat.# E6240L) and Bioo multiplex adapter for Illumina (Bioo Inc, Austin, TX USA), then sequenced on Illumina HiSeq 2000.

Park D., Shivram H, & Iyer V.R. (2014). Chd1 co-localizes with early transcription elongation factors independently of H3K36 methylation and releases stalled RNA polymerase II at introns. Epigenetics & Chromatin, 7, 32.

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Chromatin Immunoprecipitation Assay in Yeast

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Yeast cells were fixed by adding formaldehyde to cultures at a final concentration of 1% and incubating for 30 min at 30°C in a shaking incubator. Cells were then spun down, washed, and resuspended in chilled lysis buffer and subjected to bead beating at 4°C. Samples were then sonicated using a Branson Sonifier, spun down, and the supernatant was isolated. A portion of the supernatant was reserved for an input sample and the remainder was subjected to immunoprecipitation using either IgG Sepharose 6 Fast Flow beads (GE Healthcare Life Sciences) or anti-Myc conjugated agarose beads (Sigma Aldrich).

Bagchi D.N., Battenhouse A.M., Park D, & Iyer V.R. (2019). The histone variant H2A.Z in yeast is almost exclusively incorporated into the +1 nucleosome in the direction of transcription. Nucleic Acids Research, 48(1), 157-170.

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Sumoylation Status of COP1 Protein

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To determine the sumoylation status of COP1, proteins were extracted in a buffer composed of 50 mM Tris-Cl (pH 7.4), 150 mM NaCl, 1 mM EDTA (pH 8.0), 1 mM DTT, 20 mM NEM, 1% TritonX-100, and 1× complete protease inhibitor mixture (Roche, 04693159001). Then, the protein extracts were immunoprecipitated with anti-Myc-conjugated agarose beads (Sigma, F-2426) for 3 h. Next, the beads were washed with protein extraction buffer four times, and the immunoprecipitated proteins were eluted with 2× SDS loading buffer for immunoblot analysis. The sumoylated form of COP1 was identified with anti-FLAG antibody (Sigma, F3165) or anti-SUMO1 antibody (Abcam, ab5316).

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ChIP-seq of Chromatin Modifiers

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We followed the ChIP-seq protocol described in (2 ) with 150 μl of anti-Myc conjugated agarose beads (Sigma Aldrich, St Louis, MO, USA, cat.# E6654), 10 μg of H3K4me3 antibody (EMD Millipore, Darmstadt, Germany, cat.# 07–473), 10 μg of H3K36me3 antibody (Abcam, Cambridge, MA, USA, cat.# ab9050), 10 μg of RNAPII S5p antibody (Abcam, Cambridge, MA, USA, cat.# ab5131) and 10 μg of RNAPII S2p antibody (Abcam, Cambridge, MA, USA, cat.# ab5095) to pull down Chd1, H3K4me3, H3K36me3, RNAPII Ser-5P and Ser-2P, respectively. For Set2 ChIP-seq, we used the TAP-tagged Set2 strain from the TAP-tag library (15 (link)) and 100 μl of anti-TAP conjugated sepharose beads (GE Healthcare, Pittsburgh, PA, USA, cat.# 17–0969) for immunoprecipitation. For the mock ChIP, we carried out immunoprecipitation with anti-Myc conjugated agarose beads in cells expressing no Myc-tagged protein.

Lee Y., Park D, & Iyer V.R. (2017). The ATP-dependent chromatin remodeler Chd1 is recruited by transcription elongation factors and maintains H3K4me3/H3K36me3 domains at actively transcribed and spliced genes. Nucleic Acids Research, 45(12), 7180-7190.

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